Article
Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibrium.
Proceedings of the National Academy of Sciences of the United States of America - 12 Sept 1995
Phillips J P, Tainer J A, Getzoff E D, Boulianne G L, Kirby K, Hilliker A J
Abstract excerpt
Mutations in Cu/Zn superoxide dismutase (SOD), a hallmark of familial amyotrophic lateral sclerosis (FALS) in humans, are shown here to confer striking neuropathology in Drosophila. Heterozygotes with one wild-type and one deleted SOD allele retain the expected 50% of normal activity for this dimeric enzyme. However, heterozygotes with one wild-type and one missense SOD allele show lesser SOD activities, ranging...
Topics
- Amino Acid Sequence
- Amyotrophic Lateral Sclerosis
- Animals
- Base Sequence
- Drosophila melanogaster
- Heterozygote
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Mutation